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22-AUGUST-2008 06:13:22 - Amylase A diagram of an amylase molecule from human saliva. Calcium ion visible in pale khaki; chloride ion in green. From PDB 1SMD. A diagram of an amylase molecule from human saliva. Calcium ion visible in pale khaki; chloride ion in green. From PDB 1SMD. Human pancreatic amylase. Calcium ion visible in pale khaki; chloride ion in green. From PDB 1HNY. Human pancreatic amylase. Calcium ion visible in pale khaki; chloride ion in green. From PDB 1HNY. Amylase is an enzyme that breaks starch down into sugar. Amylase is present in human saliva, where it begins the chemical process of digestion. Foods that contain much starch but little sugar, such as rice and potato, taste slightly sweet as they are chewed because amylase turns some of their starch into sugar in the mouth. The pancreas also makes amylase alpha amylase to break down dietary starch into di- and trisaccharides which are converted by other enzymes to glucose to supply the body with energy. Plants and some bacteria also produce amylase. As diastase, amylase was the first enzyme to be discovered and isolated by Anselme Payen in 1833.citation needed Specific amylase proteins are designated by different Greek letters. All amylases are glycoside hydrolases and act on α-1,4-glycosidic bonds. Contents 1 Classification 1.1 α-Amylase 1.2 β-Amylase 1.3 γ-Amylase 2 Uses 3 References 4 External links Classification α-Amylase Main article: alpha-Amylase EC 3.2.1.1 CAS# 9014-71-5 alternate names: 1,4-α-D-glucan glucanohydrolase; glycogenase The α-amylases are calcium metalloenzymes, completely unable to function in the absence of calcium. By acting at random locations along the starch chain, α-amylase breaks down long-chain carbohydrates, ultimately yielding maltotriose and maltose from amylose, or maltose, glucose and limit dextrin from amylopectin. Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase. In animals, it is a major digestive enzyme and its optimum pH is 6.7-7.0. 1 In human physiology, both the salivary and pancreatic amylases are α-Amylases. They are discussed in much more detail at alpha-Amylase. Also found in plants barley , fungi ascomycetes and basidiomycetes and bacteria Bacillus β-Amylase EC 3.2.1.2 alternate names: 1,4-α-D-glucan maltohydrolase; glycogenase; saccharogen amylase Another form of amylase, β-amylase is also synthesized by bacteria, fungi, and plants. Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units maltose at a time. During the ripening of fruit, β-amylase breaks starch into sugar, resulting in the sweet flavor of ripe fruit. Both are present in seeds; β-amylase is present prior to germination, whereas α-amylase and proteases appear once germination has begun. Cereal grain amylase is key to the production of malt. Many microbes also produce amylase to degrade extracellular starches. Animal tissues do not contain β-amylase, although it may be present in microrganisms contained within the digestive tract. γ-Amylase EC 3.2.1.3 alternative names: Glucan 1,4-α-glucosidase; amyloglucosidase; Exo-1,4-α-glucosidase; glucoamylase; lysosomal α-glucosidase; 1,4-α-D-glucan glucohydrolase In addition to cleaving the last α1-4glycosidic linkages at the nonreducing end of amylose and amylopectin, yielding glucose, γ-amylase will cleave α1-6 glycosidic linkages. Unlike the other forms of amylase, γ-amylase is most efficient in acidic environments and has an optimum pH of 3 Uses Amylase enzymes are used extensively in bread making to break down complex sugars such as starch found in flour into simple sugars. Yeast then feeds on these simple sugars and converts it into the waste products of alcohol and CO2. This imparts flavour and causes the bread to rise. While Amylase enzymes are found naturally in yeast cells, it takes time for the yeast to produce enough of these enzymes to break down significant quantities of starch in the bread. This is the reason for long fermented doughs such as sour dough. Modern bread making techniques have included amylase enzymes often in the form of malted barley into bread improver thereby making the bread making process faster and more practical for commercial use.2 Bacilliary amylase is also used in detergents to dissolve starches from fabrics. Workers in factories that work with amylase for any of the above uses are at increased risk of occupational asthma. 5-9% of bakers have a positive skin test, and a fourth to a third of bakers with breathing problems are hypersensitive to amylase. 3 An inhibitor of alpha-amylase called phaseolamin has been tested as a potential diet aid. 4 References ^ Effects of pH Introduction to Enzymes ^ Maton, Anthea; Jean Hopkins, Charles William McLaughlin, Susan Johnson, Maryanna Quon Warner, David LaHart, Jill D. Wright 1993. Human Biology and Health. Englewood Cliffs, New Jersey, USA: Prentice Hall. ISBN 0-13-981176-1. ^ Mapp CE. Agents, old and new, causing occupational asthma. Occup Environ Med 2001;58:354-60. PMID 11303086. ^ Udani J, Hardy M, Madsen DC. March 2004. Blocking carbohydrate absorption and weight loss: a clinical trial using Phase 2 brand proprietary fractionated white bean extract.. Alternative medicine review. External links Molecule of the month February 2006 at the Protein Data Bank. Nutrition Sciences 101 at University of Arizona. v d e Hydrolase: sugar hydrolases EC 3.2 3.2.1: Glycoside hydrolases Amylase Alpha-Amylase - Chitinase - Lysozyme - Neuraminidase - Galactosidases Alpha, Beta - alpha-Mannosidase - Glucuronidase - Hyaluronidase - Pullulanase - Glucocerebrosidase - Galactosylceramidase - Alpha-N-acetylgalactosaminidase - Alpha-N-acetylglucosaminidase - Fucosidase - Hexosaminidase HEXA, HEXB - Iduronidase Disaccharidase Sucrase/Sucrase-isomaltase/Invertase, Maltase, Trehalase, Lactase Glucosidases Cellulase, Alpha-glucosidase, Beta-glucosidase, Debranching enzyme 3.2.2: Hydrolysing N-Glycosyl compounds DNA glycosylases: Oxoguanine glycosylase Retrieved from http://en..org/wiki/Amylase Categories: Chemical pathology | EC 3.2.1 | EnzymesHidden categories: All articles with statements | Articles with statements since June 2008 Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages ÄŒesky Dansk Deutsch Eesti Español Esperanto Français Italiano עברית Nederlands 日本語 ‪Norsk bokmÃ¥l‬ Occitan Polski Português Simple English Suomi Svenska УкраїнÑ?ька This page was last modified on 16 August 2008, at 17:34
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